|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11316 |
PRK11316 |
bifunctional D-glycero-beta-D-manno-heptose-7-phosphate kinase/D-glycero-beta-D-manno-heptose ... |
1-473 |
0e+00 |
|
bifunctional D-glycero-beta-D-manno-heptose-7-phosphate kinase/D-glycero-beta-D-manno-heptose 1-phosphate adenylyltransferase HldE;
Pssm-ID: 183085 [Multi-domain] Cd Length: 473 Bit Score: 1012.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190851 1 MKVTLPEFERAGVMVVGDVMLDRYWYGPTSRISPEAPVPVVKVDTIEERPGGAANVAMNIASLGAHSRLVGLTGIDDAAR 80
Cdd:PRK11316 1 MKVTLPDFERAGVLVVGDVMLDRYWYGPTSRISPEAPVPVVKVNQIEERPGGAANVAMNIASLGAQARLVGLTGIDEAAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190851 81 ALSKSLADVNVKCDFVSVPTHPTITKLRVLSRNQQLIRLDFEEGFEGVDPEPLHERINQALGNIGALVLSDYAKGALASV 160
Cdd:PRK11316 81 ALSKLLAAVGVKCDFVSVPTHPTITKLRVLSRNQQLIRLDFEEGFEGVDPQPLLERIEQALPSIGALVLSDYAKGALASV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190851 161 QTMIQLARKASVPVLIDPKGTDFERYRGATLLTPNLSEFEAVAGKCKTEEELVERGMKIIADFELSALLVTRSEQGMTLL 240
Cdd:PRK11316 161 QAMIQLARKAGVPVLIDPKGTDFERYRGATLLTPNLSEFEAVVGKCKDEAELVEKGMKLIADYDLSALLVTRSEQGMTLL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190851 241 QPGKAPLHMPTQAQEVYDVTGAGDTVIGVLAATLAAGNSLEEACYFANAAAGVVVGKLGTSTVSPIELENAVRGRADTGF 320
Cdd:PRK11316 241 QPGKAPLHLPTQAREVYDVTGAGDTVISVLAAALAAGNSLEEACALANAAAGVVVGKLGTSTVSPIELENALRGRAETGF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190851 321 GVMTEDELKVAVAAARKRGEKVVMTNGVFDILHAGHVSYLANARKLGDRLIVAVNSDASTKRLKGETRPVNPLEQRMIVL 400
Cdd:PRK11316 321 GVMSEEQLKLAVAQARARGEKIVMTNGCFDILHAGHVSYLANARKLGDRLIVAVNSDASVKRLKGEGRPVNPLEQRMAVL 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1513190851 401 GALEAVDWVVSFEEDTPQRLIAGILPDLLVKGGDYKPEQIAGSEEVWANGGEVMVLNFEDGCSTTNIIKKIQK 473
Cdd:PRK11316 401 AALEAVDWVVPFEEDTPQRLIAEILPDLLVKGGDYKPEEIAGSKEVWANGGEVKVLNFEDGCSTTNIIKKIRQ 473
|
|
| RfaE |
COG2870 |
ADP-heptose synthase, bifunctional sugar kinase/adenylyltransferase [Cell wall/membrane ... |
1-310 |
2.47e-168 |
|
ADP-heptose synthase, bifunctional sugar kinase/adenylyltransferase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442117 [Multi-domain] Cd Length: 321 Bit Score: 476.61 E-value: 2.47e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190851 1 MKVTLPEFERAGVMVVGDVMLDRYWYGPTSRISPEAPVPVVKVDTIEERPGGAANVAMNIASLGAHSRLVGLTGIDDAAR 80
Cdd:COG2870 6 LKELLPRFSRARVLVVGDVMLDRYWYGDVERISPEAPVPVVRVEREEERPGGAANVAANLAALGAQVTLVGVVGDDEAGR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190851 81 ALSKSLADVNVKCDFVSVPTHP-TITKLRVLSRNQQLIRLDFEEGFE--GVDPEPLHERINQALGNIGALVLSDYAKGAL 157
Cdd:COG2870 86 ELRRLLEEAGIDTDGLVVDPRRpTTTKTRVIAGGQQLLRLDFEDRFPlsAELEARLLAALEAALPEVDAVILSDYGKGVL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190851 158 AS--VQTMIQLARKASVPVLIDPKGTDFERYRGATLLTPNLSEFEAVAG-KCKTEEELVERGMKIIADFELSALLVTRSE 234
Cdd:COG2870 166 TPelIQALIALARAAGKPVLVDPKGRDFSRYRGATLLTPNLKEAEAAVGiPIADEEELVAAAAELLERLGLEALLVTRGE 245
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1513190851 235 QGMTLLQPGKAPLHMPTQAQEVYDVTGAGDTVIGVLAATLAAGNSLEEACYFANAAAGVVVGKLGTSTVSPIELEN 310
Cdd:COG2870 246 EGMTLFDADGPPHHLPAQAREVFDVTGAGDTVIATLALALAAGASLEEAAELANLAAGIVVGKLGTATVSPEELLA 321
|
|
| rfaE_dom_I |
TIGR02198 |
rfaE bifunctional protein, domain I; RfaE is a protein involved in the biosynthesis of ... |
4-313 |
4.40e-163 |
|
rfaE bifunctional protein, domain I; RfaE is a protein involved in the biosynthesis of ADP-L-glycero-D-manno-heptose, a precursor for LPS inner core biosynthesis. RfaE is a bifunctional protein in E. coli, and separate proteins in some other genome. The longer, N-terminal domain I (this family) is suggested to act in D-glycero-D-manno-heptose 1-phosphate biosynthesis, while domain II (TIGR02199) adds ADP to yield ADP-D-glycero-D-manno-heptose. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]
Pssm-ID: 274029 [Multi-domain] Cd Length: 315 Bit Score: 463.24 E-value: 4.40e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190851 4 TLPEFERAGVMVVGDVMLDRYWYGPTSRISPEAPVPVVKVDTIEERPGGAANVAMNIASLGAHSRLVGLTGIDDAARALS 83
Cdd:TIGR02198 1 LIASFKGAKVLVVGDVMLDRYWYGKVSRISPEAPVPVVKVEREEDRLGGAANVARNIASLGARVFLVGVVGDDEAGKRLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190851 84 KSLADVNVKC-DFVSVPTHPTITKLRVLSRNQQLIRLDFEE--GFEGVDPEPLHERINQALGNIGALVLSDYAKGALA-- 158
Cdd:TIGR02198 81 ALLAEEGIDTsGLIRDKDRPTTTKTRVLARNQQLLRVDFEErdPINAELEARLLAAIREQLASADAVVLSDYAKGVLTpr 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190851 159 SVQTMIQLARKASVPVLIDPKGTDFERYRGATLLTPNLSEFEAVAGKCKTEEELVERGMKIIADFELSALLVTRSEQGMT 238
Cdd:TIGR02198 161 VVQEVIAAARKHGKPVLVDPKGKDFSRYRGATLITPNRKEAEAAVGACDTEAELVQAAEKLLEELDLEALLVTRSEKGMT 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1513190851 239 LLQPGKAPLHMPTQAQEVYDVTGAGDTVIGVLAATLAAGNSLEEACYFANAAAGVVVGKLGTSTVSPIELENAVR 313
Cdd:TIGR02198 241 LFTREGEPIHIPAQAREVYDVTGAGDTVIATLALALAAGASLEEACRLANAAAGVVVGKLGTATVSPAELANALQ 315
|
|
| RfaE_like |
cd01172 |
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the ... |
13-309 |
2.28e-137 |
|
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the lipopolysaccharide (LPS) core precursor ADP-L-glycero-D-manno-heptose. LPS plays an important role in maintaining the structural integrity of the bacterial outer membrane of gram-negative bacteria. RfaE consists of two domains, a sugar kinase domain, represented here, and a domain belonging to the cytidylyltransferase superfamily.
Pssm-ID: 238577 [Multi-domain] Cd Length: 304 Bit Score: 397.32 E-value: 2.28e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190851 13 VMVVGDVMLDRYWYGPTSRISPEAPVPVVKVDTIEERPGGAANVAMNIASLGAHSRLVGLTGIDDAARALSKSLADVNVK 92
Cdd:cd01172 2 VLVVGDVILDEYLYGDVERISPEAPVPVVKVEREEIRLGGAANVANNLASLGAKVTLLGVVGDDEAGDLLRKLLEKEGID 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190851 93 CDFVSVPTHPTITKLRVLSRNQQLIRLDFEEGFEGVDPEP--LHERINQALGNIGALVLSDYAKGALA--SVQTMIQLAR 168
Cdd:cd01172 82 TDGIVDEGRPTTTKTRVIARNQQLLRVDREDDSPLSAEEEqrLIERIAERLPEADVVILSDYGKGVLTprVIEALIAAAR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190851 169 KASVPVLIDPKGTDFERYRGATLLTPNLSEFEAVAGKC-KTEEELVERGMKIIADFELSALLVTRSEQGMTLLQPGKAPL 247
Cdd:cd01172 162 ELGIPVLVDPKGRDYSKYRGATLLTPNEKEAREALGDEiNDDDELEAAGEKLLELLNLEALLVTLGEEGMTLFERDGEVQ 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1513190851 248 HMPTQAQEVYDVTGAGDTVIGVLAATLAAGNSLEEACYFANAAAGVVVGKLGTSTVSPIELE 309
Cdd:cd01172 242 HIPALAKEVYDVTGAGDTVIATLALALAAGADLEEAAFLANAAAGVVVGKVGTAPVTPKELL 303
|
|
| rfaE_dom_II |
TIGR02199 |
rfaE bifunctional protein, domain II; RfaE is a protein involved in the biosynthesis of ... |
331-473 |
3.57e-85 |
|
rfaE bifunctional protein, domain II; RfaE is a protein involved in the biosynthesis of ADP-L-glycero-D-manno-heptose, a precursor for LPS inner core biosynthesis. RfaE is a bifunctional protein in E. coli, and separate proteins in some other genome. Domain I (TIGR02198) is suggested to act in D-glycero-D-manno-heptose 1-phosphate biosynthesis, while domain II (this family) adds ADP to yield ADP-D-glycero-D-manno-heptose. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]
Pssm-ID: 131254 [Multi-domain] Cd Length: 144 Bit Score: 258.00 E-value: 3.57e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190851 331 AVAAARKRGEKVVMTNGVFDILHAGHVSYLANARKLGDRLIVAVNSDASTKRLKGETRPVNPLEQRMIVLGALEAVDWVV 410
Cdd:TIGR02199 2 LVARARARGKKIVFTNGCFDILHAGHVSYLQQARALGDRLVVGVNSDASVKRLKGETRPINPEEDRAEVLAALSSVDYVV 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1513190851 411 SFEEDTPQRLIAGILPDLLVKGGDYKPEQIAGSEEVWANGGEVMVLNFEDGCSTTNIIKKIQK 473
Cdd:TIGR02199 82 IFDEDTPEELIGELKPDILVKGGDYKVETLVGAELVESYGGQVVLLPFVEGRSTTAIIEKILK 144
|
|
| PfkB |
pfam00294 |
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ... |
13-302 |
1.97e-48 |
|
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine kinases.
Pssm-ID: 425587 [Multi-domain] Cd Length: 294 Bit Score: 168.29 E-value: 1.97e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190851 13 VMVVGDVMLDRYwygptsRISPEAPVPVVKVDTIEERPGGA-ANVAMNIASLGAHSRLVGLTGIDDAARALSKSLADVNV 91
Cdd:pfam00294 2 VVVIGEANIDLI------GNVEGLPGELVRVSTVEKGPGGKgANVAVALARLGGDVAFIGAVGDDNFGEFLLQELKKEGV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190851 92 KCDFVSV-PTHPTITKLRVLSRNQQLIRLDFEEGFEGVDPEPLhERINQALGNIGALVLSDYAKGAL--ASVQTMIQLAR 168
Cdd:pfam00294 76 DTDYVVIdEDTRTGTALIEVDGDGERTIVFNRGAAADLTPEEL-EENEDLLENADLLYISGSLPLGLpeATLEELIEAAK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190851 169 KAS--VPVLIDPKGTDFERYR----GATLLTPNLSEFEAVAGKC-KTEEELVERGMKIIADFeLSALLVTRSEQGMTLLQ 241
Cdd:pfam00294 155 NGGtfDPNLLDPLGAAREALLellpLADLLKPNEEELEALTGAKlDDIEEALAALHKLLAKG-IKTVIVTLGADGALVVE 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1513190851 242 PGKAPLHMPTQAQEVYDVTGAGDTVIGVLAATLAAGNSLEEACYFANAAAGVVVGKLGTST 302
Cdd:pfam00294 234 GDGEVHVPAVPKVKVVDTTGAGDSFVGGFLAGLLAGKSLEEALRFANAAAALVVQKSGAQT 294
|
|
| RbsK |
COG0524 |
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ... |
13-305 |
7.89e-34 |
|
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar or nucleoside kinase, ribokinase family is part of the Pathway/BioSystem: Glycolysis
Pssm-ID: 440290 [Multi-domain] Cd Length: 301 Bit Score: 129.23 E-value: 7.89e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190851 13 VMVVGDVMLDRYWYGPtsriSPEAPVPVVKVDTIEERPGG-AANVAMNIASLGAHSRLVGLTGIDDAARALSKSLADVNV 91
Cdd:COG0524 2 VLVIGEALVDLVARVD----RLPKGGETVLAGSFRRSPGGaAANVAVALARLGARVALVGAVGDDPFGDFLLAELRAEGV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190851 92 KCDFVSV-PTHPTITKLRVLSRNQQLIRLDFEEGFEGVDPEPLHErinQALGNIGALVLSDYA---KGALASVQTMIQLA 167
Cdd:COG0524 78 DTSGVRRdPGAPTGLAFILVDPDGERTIVFYRGANAELTPEDLDE---ALLAGADILHLGGITlasEPPREALLAALEAA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190851 168 RKASVPVLIDP--KGTDFERYR--------GATLLTPNLSEFEAVAGKCKTEE---ELVERGMKIIAdfelsallVTRSE 234
Cdd:COG0524 155 RAAGVPVSLDPnyRPALWEPARellrellaLVDILFPNEEEAELLTGETDPEEaaaALLARGVKLVV--------VTLGA 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1513190851 235 QGMTLLQPGKApLHMPTQAQEVYDVTGAGDTVIGVLAATLAAGNSLEEACYFANAAAGVVVGKLGTSTVSP 305
Cdd:COG0524 227 EGALLYTGGEV-VHVPAFPVEVVDTTGAGDAFAAGFLAGLLEGLDLEEALRFANAAAALVVTRPGAQPALP 296
|
|
| RfaE_N |
cd02172 |
N-terminal domain of RfaE; RfaE is a protein involved in the biosynthesis of ... |
338-471 |
2.68e-33 |
|
N-terminal domain of RfaE; RfaE is a protein involved in the biosynthesis of ADP-L-glycero-D-manno-heptose, a precursor for LPS inner core biosynthesis. RfaE is a bifunctional protein in Escherichia coli, and separate proteins in other organisms. Domain I is suggested to act in D-glycero-D-manno-heptose 1-phosphate biosynthesis, while domain II (this family) adds ADP to yield ADP-D-glycero-D-manno-heptose .
Pssm-ID: 173923 [Multi-domain] Cd Length: 144 Bit Score: 122.91 E-value: 2.68e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190851 338 RGEKVVMTNGVFDILHAGHVSYLANARKLGDRLIVAVNSDASTKRLKGetRPVNPLEQRMIVLGALEAVDWVVSFEEDTP 417
Cdd:cd02172 2 RGKTVVLCHGVFDLLHPGHVRHLQAARSLGDILVVSLTSDRYVNKGPG--RPIFPEDLRAEVLAALGFVDYVVLFDNPTA 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1513190851 418 QRLIAGILPDLLVKGGDYK-------PEQIAGSEEVWANGGEvMVLNFEDGCSTTNIIKKI 471
Cdd:cd02172 80 LEIIDALQPNIYVKGGDYEnpendvtGKIAPEAEAVKAYGGK-IVFTGEIVFSSSALINRI 139
|
|
| TagD |
COG0615 |
Glycerol-3-phosphate cytidylyltransferase, cytidylyltransferase family [Cell wall/membrane ... |
341-471 |
1.28e-29 |
|
Glycerol-3-phosphate cytidylyltransferase, cytidylyltransferase family [Cell wall/membrane/envelope biogenesis]; Glycerol-3-phosphate cytidylyltransferase, cytidylyltransferase family is part of the Pathway/BioSystem: Riboflavin/FAD biosynthesis
Pssm-ID: 440380 [Multi-domain] Cd Length: 131 Bit Score: 112.50 E-value: 1.28e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190851 341 KVVMTNGVFDILHAGHVSYLANARKLGDRLIVAVNSDaSTKRLKGEtRPVNPLEQRMIVLGALEAVDWVVSFEEDTPQRL 420
Cdd:COG0615 1 KRVITYGTFDLLHPGHINLLKRAKALGDELIVGVATD-EFVASKGR-KPIIPEEQRKEIVEALKYVDEVILGEEWDKFED 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1513190851 421 IAGILPDLLVKGGD--YKPEQIAGSEEVWANGGEVMVLNFEDGCSTTNIIKKI 471
Cdd:COG0615 79 IEEIKPDVIVLGDDwkGDFDFLKEELEKRGIGCEVVYLPRTEGISSTKIKKRI 131
|
|
| cytidylyltransferase |
cd02170 |
cytidylyltransferase; The cytidylyltransferase family includes cholinephosphate ... |
340-473 |
1.15e-24 |
|
cytidylyltransferase; The cytidylyltransferase family includes cholinephosphate cytidylyltransferase (CCT), glycerol-3-phosphate cytidylyltransferase, RafE and phosphoethanolamine cytidylyltransferase (ECT). All enzymes catalyze the transfer of a cytidylyl group from CTP to various substrates.
Pssm-ID: 173921 [Multi-domain] Cd Length: 136 Bit Score: 98.90 E-value: 1.15e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190851 340 EKVVMTNGVFDILHAGHVSYLANARKLGDRLIVAVNSDASTKRLKGetRPVNPLEQRMIVLGALEAVDWVVSFEEDTPQR 419
Cdd:cd02170 1 MKRVYAAGTFDIIHPGHIRFLEEAKKLGDYLIVGVARDETVAKIKR--RPILPEEQRAEVVEALKYVDEVILGHPWSYFK 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1513190851 420 LIAGILPDLLVKGGDYK-PEQIAGSEEVWANGGEVMVLNFED--GCSTTNIIKKIQK 473
Cdd:cd02170 79 PLEELKPDVIVLGDDQKnGVDEEEVYEELKKRGKVIEVPRKKteGISSSDIIKRILE 135
|
|
| ribokinase |
cd01174 |
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ... |
12-300 |
3.24e-22 |
|
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This reaction is the first step in the ribose metabolism. It traps ribose within the cell after uptake and also prepares the sugar for use in the synthesis of nucleotides and histidine, and for entry into the pentose phosphate pathway. Ribokinase is dimeric in solution.
Pssm-ID: 238579 [Multi-domain] Cd Length: 292 Bit Score: 96.47 E-value: 3.24e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190851 12 GVMVVGDVMLDRYWYgpTSRIspeaPVP--VVKVDTIEERPGG-AANVAMNIASLGAHSRLVGLTGIDDAARALSKSLAD 88
Cdd:cd01174 1 KVVVVGSINVDLVTR--VDRL----PKPgeTVLGSSFETGPGGkGANQAVAAARLGARVAMIGAVGDDAFGDELLENLRE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190851 89 VNVKCDFVS-VPTHPTITKLRVLS---RNQQLI------RLDFEegfegvDPEPLHERINQAlgniGALVL----Sdyak 154
Cdd:cd01174 75 EGIDVSYVEvVVGAPTGTAVITVDesgENRIVVvpgangELTPA------DVDAALELIAAA----DVLLLqleiP---- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190851 155 gaLASVQTMIQLARKASVPVLIDP---KGTDFERYRGATLLTPNLSEFEAVAGKCKTEEELVERGMKIIADFELSALLVT 231
Cdd:cd01174 141 --LETVLAALRAARRAGVTVILNPapaRPLPAELLALVDILVPNETEAALLTGIEVTDEEDAEKAARLLLAKGVKNVIVT 218
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1513190851 232 RSEQGMTLLQPGKaPLHMPTQAQEVYDVTGAGDTVIGVLAATLAAGNSLEEACYFANAAAGVVVGKLGT 300
Cdd:cd01174 219 LGAKGALLASGGE-VEHVPAFKVKAVDTTGAGDTFIGALAAALARGLSLEEAIRFANAAAALSVTRPGA 286
|
|
| bac_FRK |
cd01167 |
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for ... |
13-299 |
1.28e-20 |
|
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for fructose, as are all FRKs, but they catalyzes the conversion of fructose to fructose-6-phosphate, which is an entry point into glycolysis via conversion into glucose-6-phosphate. This is in contrast to FRKs [or ketohexokinases (KHKs)] from mammalia and halophilic archaebacteria, which phosphorylate fructose to fructose-1-phosphate.
Pssm-ID: 238572 [Multi-domain] Cd Length: 295 Bit Score: 91.93 E-value: 1.28e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190851 13 VMVVGDVMLDRYwygptsrispeaPVPVVKVDTIEERPGGA-ANVAMNIASLGAHSRLVGLTGIDDAARALSKSLADVNV 91
Cdd:cd01167 2 VVCFGEALIDFI------------PEGSGAPETFTKAPGGApANVAVALARLGGKAAFIGKVGDDEFGDFLLETLKEAGV 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190851 92 KCDFV-SVPTHPTITKLRVLSRNQQLIrldfeegFEGVDPEP----LHERINQALGN------IGALVLSDyAKGALASV 160
Cdd:cd01167 70 DTRGIqFDPAAPTTLAFVTLDADGERS-------FEFYRGPAadllLDTELNPDLLSeadilhFGSIALAS-EPSRSALL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190851 161 QTMiQLARKASVPVLIDPKgtdfER---YRGATLLTPNLSEFEAVAGKCK-TEEELV--------ERGMKIIADFELSAL 228
Cdd:cd01167 142 ELL-EAAKKAGVLISFDPN----LRpplWRDEEEARERIAELLELADIVKlSDEELEllfgeedpEEIAALLLLFGLKLV 216
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1513190851 229 LVTRSEQGMTLLQPGKaPLHMPTQAQEVYDVTGAGDTVIGVLAATLAAGNS-------LEEACYFANAAAGVVVGKLG 299
Cdd:cd01167 217 LVTRGADGALLYTKGG-VGEVPGIPVEVVDTTGAGDAFVAGLLAQLLSRGLlaldedeLAEALRFANAVGALTCTKAG 293
|
|
| YeiC_kinase_like |
cd01941 |
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ... |
13-291 |
4.20e-20 |
|
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ribokinase/pfkB sugar kinase superfamily. Its oligomerization state is unknown at this time.
Pssm-ID: 238916 [Multi-domain] Cd Length: 288 Bit Score: 90.07 E-value: 4.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190851 13 VMVVGDVMLDRYWYgPTSRISPEAPVPVvkvdTIEERPGGAA-NVAMNIASLGAHSRLVGLTGIDDAARALSKSLADVNV 91
Cdd:cd01941 2 IVVIGAANIDLRGK-VSGSLVPGTSNPG----HVKQSPGGVGrNIAENLARLGVSVALLSAVGDDSEGESILEESEKAGL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190851 92 KCDFVSVPTHPTITKLRVLSRNQQLI------RLdFEEGFEGVDPEpLHERINQAL-----GNIGALVLsdyakgalasv 160
Cdd:cd01941 77 NVRGIVFEGRSTASYTAILDKDGDLVvaladmDI-YELLTPDFLRK-IREALKEAKpivvdANLPEEAL----------- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190851 161 QTMIQLARKASVPVLIDPKGTD-----FERYRGATLLTPNLSEFEAVAGKCKTEEELVERGMKIIADFELSALLVTRSEQ 235
Cdd:cd01941 144 EYLLALAAKHGVPVAFEPTSAPklkklFYLLHAIDLLTPNRAELEALAGALIENNEDENKAAKILLLPGIKNVIVTLGAK 223
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1513190851 236 G--MTLLQPGKAPLHMPT-QAQEVYDVTGAGDTVIGVLAATLAAGNSLEEACYFANAAA 291
Cdd:cd01941 224 GvlLSSREGGVETKLFPApQPETVVNVTGAGDAFVAGLVAGLLEGMSLDDSLRFAQAAA 282
|
|
| CTP_transf_like |
pfam01467 |
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; ... |
344-470 |
7.82e-19 |
|
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; glycerol-3-phosphate cytidylyltransferase. It also includes putative adenylyltransferases, and FAD synthases.
Pssm-ID: 396172 [Multi-domain] Cd Length: 134 Bit Score: 82.37 E-value: 7.82e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190851 344 MTNGVFDILHAGHVSYLANARKLGDR-LIVAVNSDASTKRLKgetRPVNPLEQRMIVLGALEAVDWVVSFEEDTPQRLIA 422
Cdd:pfam01467 1 LFGGTFDPIHLGHLRLLEQAKELFDEdLIVGVPSDEPPHKLK---RPLFSAEERLEMLELAKWVDEVIVVAPWELTRELL 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1513190851 423 GIL-PDLLVKGGDYKPEQIAGSEEVWANGGEV--------MVLNFEDGCSTTNIIKK 470
Cdd:pfam01467 78 KELnPDVLVIGADSLLDFWYELDEILGNVKLVvvvrpvffIPLKPTNGISSTDIRER 134
|
|
| FruK |
COG1105 |
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism]; |
40-305 |
1.71e-18 |
|
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
Pssm-ID: 440722 [Multi-domain] Cd Length: 304 Bit Score: 85.96 E-value: 1.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190851 40 VVKVDTIEERPGG-AANVAMNIASLGAHSRLVGLTGiDDAARALSKSLADVNVKCDFVSVPTH-PTITKLRVLSRNQQLi 117
Cdd:COG1105 24 VNRASEVRLDPGGkGINVARVLKALGVDVTALGFLG-GFTGEFIEELLDEEGIPTDFVPIEGEtRINIKIVDPSDGTET- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190851 118 rlDF-EEGFEgVDPE---PLHERINQALGNIGALVLSdyakGALAS------VQTMIQLARKASVPVLIDPKGTDFE--- 184
Cdd:COG1105 102 --EInEPGPE-ISEEeleALLERLEELLKEGDWVVLS----GSLPPgvppdfYAELIRLARARGAKVVLDTSGEALKaal 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190851 185 RYrGATLLTPNLSEFEAVAG-KCKTEEE-------LVERGMKIIadfelsalLVTRSEQGMTLLQPGKApLHMPTQAQEV 256
Cdd:COG1105 175 EA-GPDLIKPNLEELEELLGrPLETLEDiiaaareLLERGAENV--------VVSLGADGALLVTEDGV-YRAKPPKVEV 244
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1513190851 257 YDVTGAGDTVIGVLAATLAAGNSLEEACYFANAAAGVVVGKLGTSTVSP 305
Cdd:COG1105 245 VSTVGAGDSMVAGFLAGLARGLDLEEALRLAVAAGAAAALSPGTGLPDR 293
|
|
| cyt_tran_rel |
TIGR00125 |
cytidyltransferase-like domain; Protein families that contain at least one copy of this domain ... |
342-409 |
6.45e-18 |
|
cytidyltransferase-like domain; Protein families that contain at least one copy of this domain include citrate lyase ligase, pantoate-beta-alanine ligase, glycerol-3-phosphate cytidyltransferase, ADP-heptose synthase, phosphocholine cytidylyltransferase, lipopolysaccharide core biosynthesis protein KdtB, the bifunctional protein NadR, and a number whose function is unknown. Many of these proteins are known to use CTP or ATP and release pyrophosphate.
Pssm-ID: 272920 [Multi-domain] Cd Length: 66 Bit Score: 77.73 E-value: 6.45e-18
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1513190851 342 VVMTNGVFDILHAGHVSYLANARKLGDRLIVAVNSDASTKRLKGEtrPVNPLEQRMIVLGALEAVDWV 409
Cdd:TIGR00125 1 RVIFVGTFDPFHLGHLDLLERAKELFDELIVGVGSDQFVNPLKGE--PVFSLEERLEMLKALKYVDEV 66
|
|
| ribokinase_pfkB_like |
cd00287 |
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ... |
13-275 |
1.62e-17 |
|
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including carbohydrates and aromatic small molecules, all are phosphorylated at a hydroxyl group. The superfamily includes ribokinase, fructokinase, ketohexokinase, 2-dehydro-3-deoxygluconokinase, 1-phosphofructokinase, the minor 6-phosphofructokinase (PfkB), inosine-guanosine kinase, and adenosine kinase. Even though there is a high degree of structural conservation within this superfamily, their multimerization level varies widely, monomeric (e.g. adenosine kinase), dimeric (e.g. ribokinase), and trimeric (e.g THZ kinase).
Pssm-ID: 238177 [Multi-domain] Cd Length: 196 Bit Score: 80.60 E-value: 1.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190851 13 VMVVGDVMLDRYWYGPTSrisPEAPVPVVKVDTIEERPGGAANVAMNIASLGAHSRLVGltgiddaaralsksladvnvk 92
Cdd:cd00287 2 VLVVGSLLVDVILRVDAL---PLPGGLVRPGDTEERAGGGAANVAVALARLGVSVTLVG--------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190851 93 cdfvsvpthptitklrvlsrnqqlirldfeegfegvdpeplherinqalgnIGALVLSDYAKgALASVQTMIQLARKASV 172
Cdd:cd00287 58 ---------------------------------------------------ADAVVISGLSP-APEAVLDALEEARRRGV 85
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190851 173 PVLIDP--------KGTDFERYRGATLLTPNLSEFEAVAGKCKTEEELVERGMKIIADFELSALLVTRSEQGMTLLQPGK 244
Cdd:cd00287 86 PVVLDPgpravrldGEELEKLLPGVDILTPNEEEAEALTGRRDLEVKEAAEAAALLLSKGPKVVIVTLGEKGAIVATRGG 165
|
250 260 270
....*....|....*....|....*....|.
gi 1513190851 245 APLHMPTQAQEVYDVTGAGDTVIGVLAATLA 275
Cdd:cd00287 166 TEVHVPAFPVKVVDTTGAGDAFLAALAAGLA 196
|
|
| KdgK |
cd01166 |
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ... |
13-299 |
2.98e-16 |
|
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form 2-keto-3-deoxy-6-phosphogluconate (KDGP). KDG is the common intermediate product, that allows organisms to channel D-glucuronate and/or D-galacturinate into the glycolysis and therefore use polymers, like pectin and xylan as carbon sources.
Pssm-ID: 238571 [Multi-domain] Cd Length: 294 Bit Score: 79.16 E-value: 2.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190851 13 VMVVGDVMLdrywygptsRISPEAPVPVVKVDTIEERPGGA-ANVAMNIASLGAHSRLVGLTGIDDAARALSKSLADVNV 91
Cdd:cd01166 2 VVTIGEVMV---------DLSPPGGGRLEQADSFRKFFGGAeANVAVGLARLGHRVALVTAVGDDPFGRFILAELRREGV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190851 92 KCDFVSV-PTHPTITklrvlsrnqQLIRLDFEEGFEGV-----------DPEPLHERinqALGNIGALVLSDYA----KG 155
Cdd:cd01166 73 DTSHVRVdPGRPTGL---------YFLEIGAGGERRVLyyragsaasrlTPEDLDEA---ALAGADHLHLSGITlalsES 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190851 156 ALASVQTMIQLARKASVPVLID----PKGTDFERYR--------GATLLTPNLSEFEAVAGkCKTEEELVERGMKIiaDF 223
Cdd:cd01166 141 AREALLEALEAAKARGVTVSFDlnyrPKLWSAEEARealeellpYVDIVLPSEEEAEALLG-DEDPTDAAERALAL--AL 217
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1513190851 224 ELSALLVTRSEQGMTLLQPGKApLHMPTQAQEVYDVTGAGDTVIGVLAATLAAGNSLEEACYFANAAAGVVVGKLG 299
Cdd:cd01166 218 GVKAVVVKLGAEGALVYTGGGR-VFVPAYPVEVVDTTGAGDAFAAGFLAGLLEGWDLEEALRFANAAAALVVTRPG 292
|
|
| ribokinase_group_A |
cd01942 |
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ... |
13-301 |
9.24e-16 |
|
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ribokinase/pfkB superfamily. Its oligomerization state is unknown at this time.
Pssm-ID: 238917 [Multi-domain] Cd Length: 279 Bit Score: 77.35 E-value: 9.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190851 13 VMVVGDVMLDRYWYGPTSrisPEAPVPVVkVDTIEERPGG-AANVAMNIASLGAHSRLVGLTGIDDAARALSKSLADVNV 91
Cdd:cd01942 2 VAVVGHLNYDIILKVESF---PGPFESVL-VKDLRREFGGsAGNTAVALAKLGLSPGLVAAVGEDFHGRLYLEELREEGV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190851 92 KCDFV--SVPTHPTITKLRVLSRNQQLIRLDfeegfEGVDPEPLHERINQALGNIGALvlsdyakgALASVQTMIQLAR- 168
Cdd:cd01942 78 DTSHVrvVDEDSTGVAFILTDGDDNQIAYFY-----PGAMDELEPNDEADPDGLADIV--------HLSSGPGLIELARe 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190851 169 --KASVPVLIDPkGTDFERYRGATL---------LTPNLSEFEAVAGKCKTEEELVERGMKIIadfelsalLVTRSEQGM 237
Cdd:cd01942 145 laAGGITVSFDP-GQELPRLSGEELeeileradiLFVNDYEAELLKERTGLSEAELASGVRVV--------VVTLGPKGA 215
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1513190851 238 TLLQPGKAPLHMPTQAQEVYDVTGAGDTVIGVLAATLAAGNSLEEACYFANAAAGVVVGKLGTS 301
Cdd:cd01942 216 IVFEDGEEVEVPAVPAVKVVDTTGAGDAFRAGFLYGLLRGYDLEESLRLGNLAASLKVERRGAQ 279
|
|
| FruK_PfkB_like |
cd01164 |
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. ... |
40-300 |
3.47e-14 |
|
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. FruK plays an important role in the predominant pathway for fructose utilisation.This group also contains tagatose-6-phophate kinase, an enzyme of the tagatose 6-phosphate pathway, which responsible for breakdown of the galactose moiety during lactose metabolism by bacteria such as L. lactis.
Pssm-ID: 238570 [Multi-domain] Cd Length: 289 Bit Score: 72.95 E-value: 3.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190851 40 VVKVDTIEERPGG-AANVAMNIASLGAHSRLVGLTGiDDAARALSKSLADVNVKCDFVSVPThPTITKLRVLSRNQQLIR 118
Cdd:cd01164 25 VNRVSSTRKDAGGkGINVARVLKDLGVEVTALGFLG-GFTGDFFEALLKEEGIPDDFVEVAG-ETRINVKIKEEDGTETE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190851 119 LDfEEGFEgVDPEPLH---ERINQALGNIGALVLSdyakGALAS------VQTMIQLARKASVPVLIDpkgTDFERYR-- 187
Cdd:cd01164 103 IN-EPGPE-ISEEELEallEKLKALLKKGDIVVLS----GSLPPgvpadfYAELVRLAREKGARVILD---TSGEALLaa 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190851 188 ---GATLLTPNLSEFEAVAGK-CKTEEELVERGMKIIADfELSALLVTRSEQGMTLLQPGKApLHMPTQAQEVYDVTGAG 263
Cdd:cd01164 174 laaKPFLIKPNREELEELFGRpLGDEEDVIAAARKLIER-GAENVLVSLGADGALLVTKDGV-YRASPPKVKVVSTVGAG 251
|
250 260 270
....*....|....*....|....*....|....*..
gi 1513190851 264 DTVIGVLAATLAAGNSLEEACYFANAAAGVVVGKLGT 300
Cdd:cd01164 252 DSMVAGFVAGLAQGLSLEEALRLAVAAGSATAFSPGT 288
|
|
| G3P_Cytidylyltransferase |
cd02171 |
glycerol-3-phosphate cytidylyltransferase; Glycerol-3-phosphate cytidylyltransferase, ... |
340-473 |
2.00e-13 |
|
glycerol-3-phosphate cytidylyltransferase; Glycerol-3-phosphate cytidylyltransferase,(CDP-glycerol pyrophosphorylase). Glycerol-3-phosphate cytidyltransferase acts in pathways of teichoic acid biosynthesis. Teichoic acids are substituted polymers, linked by phosphodiester bonds, of glycerol, ribitol, etc. An example is poly(glycerol phosphate), the major teichoic acid of the Bacillus subtilis cell wall. Most, but not all, species encoding proteins in this family are Gram-positive bacteria. A closely related protein assigned a different function experimentally is a human ethanolamine-phosphate cytidylyltransferase.
Pssm-ID: 173922 [Multi-domain] Cd Length: 129 Bit Score: 67.12 E-value: 2.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190851 340 EKVVMTNGVFDILHAGHVSYLANARKLGDRLIVAVNSDaSTKRLKGEtRPVNPLEQRMIVLGALEAVDWVVSfEEDTPQR 419
Cdd:cd02171 1 MKVVITYGTFDLLHIGHLNLLERAKALGDKLIVAVSTD-EFNAGKGK-KAVIPYEQRAEILESIRYVDLVIP-ETNWEQK 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1513190851 420 L--IAGILPDLLVKGGDYKpeqiaGSEEVWANGGEVMVLNFEDGCSTTNIIKKIQK 473
Cdd:cd02171 78 IedIKKYNVDVFVMGDDWE-----GKFDFLKEYCEVVYLPRTKGISSTQLKEMLKK 128
|
|
| ECT |
cd02173 |
CTP:phosphoethanolamine cytidylyltransferase (ECT); CTP:phosphoethanolamine ... |
339-473 |
1.03e-12 |
|
CTP:phosphoethanolamine cytidylyltransferase (ECT); CTP:phosphoethanolamine cytidylyltransferase (ECT) catalyzes the conversion of phosphoethanolamine to CDP-ethanolamine as part of the CDP-ethanolamine biosynthesis pathway. ECT expression in hepatocytes is localized predominantly to areas of the cytoplasm that are rich in rough endoplasmic reticulum. Several ECTs, including yeast and human ECT, have large repetitive sequences located within their N- and C-termini.
Pssm-ID: 173924 Cd Length: 152 Bit Score: 65.74 E-value: 1.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190851 339 GEKVVMTNGVFDILHAGHVSYLANARKLGDRLIVAVNSDASTKRLKGETRPV-NPLEQRMIVLgALEAVDWVV-----SF 412
Cdd:cd02173 1 GDKVVYVDGAFDLFHIGHIEFLEKARELGDYLIVGVHDDQTVNEYKGSNYPImNLHERVLSVL-ACRYVDEVVigapyVI 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1513190851 413 EEDtpqrLIAGILPDLLVKGGDYKPEQIAGSEEVWA---NGGEVMVLNFEDGCSTTNIIKKIQK 473
Cdd:cd02173 80 TKE----LIEHFKIDVVVHGKTEETPDSLDGEDPYAvpkEMGIFKEIDSGSDLTTRDIVNRIIK 139
|
|
| PLN02406 |
PLN02406 |
ethanolamine-phosphate cytidylyltransferase |
336-471 |
7.41e-12 |
|
ethanolamine-phosphate cytidylyltransferase
Pssm-ID: 215227 [Multi-domain] Cd Length: 418 Bit Score: 67.01 E-value: 7.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190851 336 RKRGEKVVMtNGVFDILHAGHVSYLANARKLGDRLIVAVNSDASTKRLKGEtrPVNPLEQRMIVLGALEAVDWVVS---- 411
Cdd:PLN02406 50 KKKPVRVYM-DGCFDMMHYGHANALRQARALGDELVVGVVSDEEIIANKGP--PVTPMHERMIMVSGVKWVDEVIPdapy 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190851 412 ----------FEEDTPQRLIAG----ILPD------LLVKGGDYKpeQIAGSEevwanggevmvlnfedGCSTTNIIKKI 471
Cdd:PLN02406 127 aiteefmnklFNEYNIDYIIHGddpcLLPDgtdayaLAKKAGRYK--QIKRTE----------------GVSSTDIVGRM 188
|
|
| ribokinase_group_B |
cd01945 |
Ribokinase-like subgroup B. Found in bacteria and plants, this subgroup is part of the ... |
51-305 |
1.44e-11 |
|
Ribokinase-like subgroup B. Found in bacteria and plants, this subgroup is part of the ribokinase/pfkB superfamily. Its oligomerization state is unknown at this time. .
Pssm-ID: 238920 [Multi-domain] Cd Length: 284 Bit Score: 65.01 E-value: 1.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190851 51 GGAANVAMNIASLGAHSRLVGLTGIDDAARALSKSLADVNVKCDFV-----SVPTHPTITKLRVLSRNQQLIRLDFEEgf 125
Cdd:cd01945 37 GNAANAAVAVARLGGQARLIGVVGDDAIGRLILAELAAEGVDTSFIvvapgARSPISSITDITGDRATISITAIDTQA-- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190851 126 egvDPEPLHERInqaLGNIGALVLSDYAKGALASVqtmIQLARKASVPVLIDPKGTDFERYRGATLLTPNL--SEfEAVA 203
Cdd:cd01945 115 ---APDSLPDAI---LGGADAVLVDGRQPEAALHL---AQEARARGIPIPLDLDGGGLRVLEELLPLADHAicSE-NFLR 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190851 204 GKCKTEEELVergMKIIADFELSALLVTRSEQGMTLLQPGKAPLHMPTQAQEVYDVTGAGDTVIGVLAATLAAGNSLEEA 283
Cdd:cd01945 185 PNTGSADDEA---LELLASLGIPFVAVTLGEAGCLWLERDGELFHVPAFPVEVVDTTGAGDVFHGAFAHALAEGMPLREA 261
|
250 260
....*....|....*....|..
gi 1513190851 284 CYFANAAAGVVVGKLGTSTVSP 305
Cdd:cd01945 262 LRFASAAAALKCRGLGGRAGLP 283
|
|
| PTZ00308 |
PTZ00308 |
ethanolamine-phosphate cytidylyltransferase; Provisional |
337-474 |
3.82e-11 |
|
ethanolamine-phosphate cytidylyltransferase; Provisional
Pssm-ID: 140329 [Multi-domain] Cd Length: 353 Bit Score: 64.42 E-value: 3.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190851 337 KRGEKVVMTNGVFDILHAGHVSYLANARKLGDRLIVAVNSDASTKRLKGETRPVNPLEQRmiVLGALEA--VDWVV-SFE 413
Cdd:PTZ00308 189 KPGDRIVYVDGSFDLFHIGHIRVLQKARELGDYLIVGVHEDQVVNEQKGSNYPIMNLNER--VLGVLSCryVDEVViGAP 266
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1513190851 414 EDTPQRLIAGILPDLLVKGGDYKPEQIAGSEEVWANGGEVMVL-NFEDGC--STTNIIKKIQKD 474
Cdd:PTZ00308 267 FDVTKEVIDSLHINVVVGGKFSDLVNEEGGSDPYEVPKAMGIFkEVDSGCdlTTDSIVDRVVKN 330
|
|
| PTZ00292 |
PTZ00292 |
ribokinase; Provisional |
51-305 |
4.67e-11 |
|
ribokinase; Provisional
Pssm-ID: 185541 [Multi-domain] Cd Length: 326 Bit Score: 63.99 E-value: 4.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190851 51 GGAANVAMNIASLGAHSRLVGLTGIDDAARALSKSLADVNVKCDFVSVpthptitkLRVLSRNQQLIRLDFEEG------ 124
Cdd:PTZ00292 53 GKGANQAVMASKLGAKVAMVGMVGTDGFGSDTIKNFKRNGVNTSFVSR--------TENSSTGLAMIFVDTKTGnneivi 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190851 125 ----FEGVDPEPLHERINQaLGNIGALVL--------SDYA---KGALASVQTMIQLArkASVPVLIDPKGTDFERYrgA 189
Cdd:PTZ00292 125 ipgaNNALTPQMVDAQTDN-IQNICKYLIcqneipleTTLDalkEAKERGCYTVFNPA--PAPKLAEVEIIKPFLKY--V 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190851 190 TLLTPNLSEFEAVAGKCKTEEELVERGMKIIADFELSALLVTRSEQGMTLLQPGKAPLHMPTQAQEVYDVTGAGDTVIGV 269
Cdd:PTZ00292 200 SLFCVNEVEAALITGMEVTDTESAFKASKELQQLGVENVIITLGANGCLIVEKENEPVHVPGKRVKAVDTTGAGDCFVGS 279
|
250 260 270
....*....|....*....|....*....|....*.
gi 1513190851 270 LAATLAAGNSLEEACYFANAAAGVVVGKLGTSTVSP 305
Cdd:PTZ00292 280 MAYFMSRGKDLKESCKRANRIAAISVTRHGTQSSYP 315
|
|
| CCT |
cd02174 |
CTP:phosphocholine cytidylyltransferase; CTP:phosphocholine cytidylyltransferase (CCT) ... |
347-417 |
5.99e-11 |
|
CTP:phosphocholine cytidylyltransferase; CTP:phosphocholine cytidylyltransferase (CCT) catalyzes the condensation of CTP and phosphocholine to form CDP-choline as the rate-limiting and regulatory step in the CDP-choline pathway. CCT is unique in that its enzymatic activity is regulated by the extent of its association with membrane structures. A current model posts that the elastic stress of the bilayer curvature is sensed by CCT and this governs the degree of membrane association, thus providing a mechanism for both positive and negative regulation of activity.
Pssm-ID: 173925 Cd Length: 150 Bit Score: 60.66 E-value: 5.99e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1513190851 347 GVFDILHAGHVSYLANARKLG--DRLIVAVNSDASTKRLKGetRPVNPLEQRMIVLGALEAVDWVVsfeEDTP 417
Cdd:cd02174 9 GCFDLFHYGHANALRQAKKLGpnDYLIVGVHSDEEIHKHKG--PPVMTEEERYEAVRHCKWVDEVV---EGAP 76
|
|
| adenosine_kinase |
cd01168 |
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside ... |
15-301 |
3.68e-10 |
|
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside analogues at the 5'-hydroxyl using ATP or GTP as the phosphate donor.The physiological function of AK is associated with the regulation of extracellular adenosine levels and the preservation of intracellular adenylate pools. Adenosine kinase is involved in the purine salvage pathway.
Pssm-ID: 238573 [Multi-domain] Cd Length: 312 Bit Score: 61.09 E-value: 3.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190851 15 VVGDVMLDRYWYGPTSRISPEAPV--PVVKVDTIEERPGG-AANVAMNIASLGAHSRLVGLTGIDDAARALSKSLADVNV 91
Cdd:cd01168 17 QVDDAFLEKLGLKKGDMILADMEEqeELLAKLPVKYIAGGsAANTIRGAAALGGSAAFIGRVGDDKLGDFLLKDLRAAGV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190851 92 KCDFVSVPTHPTitklrvlSRNQQLIRLDFEEG---FEGVDPEPLHERINQALgnI-GALVLsdYAKGAL-----ASVQT 162
Cdd:cd01168 97 DTRYQVQPDGPT-------GTCAVLVTPDAERTmctYLGAANELSPDDLDWSL--LaKAKYL--YLEGYLltvppEAILL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190851 163 MIQLARKASVPV---LIDPKGTDFerYR--------GATLLTPNLSEFEAVAGKCKTEEELVERGmkiIADFELSALLVT 231
Cdd:cd01168 166 AAEHAKENGVKIalnLSAPFIVQR--FKeallellpYVDILFGNEEEAEALAEAETTDDLEAALK---LLALRCRIVVIT 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1513190851 232 RSEQGMTLLQPGKApLHMPTQAQE-VYDVTGAGDT-VIGVLAAtLAAGNSLEEACYFANAAAGVVVGKLGTS 301
Cdd:cd01168 241 QGAKGAVVVEGGEV-YPVPAIPVEkIVDTNGAGDAfAGGFLYG-LVQGEPLEECIRLGSYAAAEVIQQLGPR 310
|
|
| YegV_kinase_like |
cd01944 |
YegV-like sugar kinase. Found only in bacteria, YegV-like kinase is part of the ribokinase ... |
150-299 |
5.59e-10 |
|
YegV-like sugar kinase. Found only in bacteria, YegV-like kinase is part of the ribokinase/pfkB sugar kinase superfamily. Its oligomerization state is unknown at this time.
Pssm-ID: 238919 [Multi-domain] Cd Length: 289 Bit Score: 60.13 E-value: 5.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190851 150 SDYAKGALASVQTMIQlarkASVPVLIDPKGTDFERYR--------GATLLTPNLSEFEAVAGKCKTEEELVERGMKIia 221
Cdd:cd01944 139 ENASKVILLEWLEALP----AGTTLVFDPGPRISDIPDtilqalmaKRPIWSCNREEAAIFAERGDPAAEASALRIYA-- 212
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1513190851 222 dfELSALLVTRS-EQGMTLLQPGKAPLHMPTQAQEVYDVTGAGDTVIGVLAATLAAGNSLEEACYFANAAAGVVVGKLG 299
Cdd:cd01944 213 --KTAAPVVVRLgSNGAWIRLPDGNTHIIPGFKVKAVDTIGAGDTHAGGMLAGLAKGMSLADAVLLANAAAAIVVTRSG 289
|
|
| PLN02406 |
PLN02406 |
ethanolamine-phosphate cytidylyltransferase |
341-410 |
7.82e-09 |
|
ethanolamine-phosphate cytidylyltransferase
Pssm-ID: 215227 [Multi-domain] Cd Length: 418 Bit Score: 57.38 E-value: 7.82e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190851 341 KVVMTNGVFDILHAGHVSYLANARKLGDRLIVAVNSDASTKRLKGETRPVNPLEQRMIVLGALEAVDWVV 410
Cdd:PLN02406 252 RIVYIDGAFDLFHAGHVEILRLARALGDFLLVGIHTDQTVSAHRGAHRPIMNLHERSLSVLACRYVDEVI 321
|
|
| PTZ00308 |
PTZ00308 |
ethanolamine-phosphate cytidylyltransferase; Provisional |
333-417 |
1.21e-08 |
|
ethanolamine-phosphate cytidylyltransferase; Provisional
Pssm-ID: 140329 [Multi-domain] Cd Length: 353 Bit Score: 56.72 E-value: 1.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190851 333 AAARKRGEKVVMTNGVFDILHAGHVSYLANARKLGDRLIVAVNSDASTKRLKGEtrPVNPLEQRMIVLGALEAVDWVVsf 412
Cdd:PTZ00308 4 IPPKKPGTIRVWVDGCFDMLHFGHANALRQARALGDELFVGCHSDEEIMRNKGP--PVMHQEERYEALRACKWVDEVV-- 79
|
....*
gi 1513190851 413 eEDTP 417
Cdd:PTZ00308 80 -EGYP 83
|
|
| Guanosine_kinase_like |
cd01947 |
Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like ... |
13-299 |
1.40e-08 |
|
Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like group is part of the ribokinase/pfkB sugar kinase superfamily. Its oligomerization state is unknown at this time.
Pssm-ID: 238922 [Multi-domain] Cd Length: 265 Bit Score: 55.89 E-value: 1.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190851 13 VMVVGDVMLDRYWYGPtsriSPEAPVPVVKVDTIEERPGGA-ANVAMNIASLGAHSRLVGLTGIDDAARALSKSLADVNV 91
Cdd:cd01947 2 IAVVGHVEWDIFLSLD----APPQPGGISHSSDSRESPGGGgANVAVQLAKLGNDVRFFSNLGRDEIGIQSLEELESGGD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190851 92 kCDFVSVPTHPTITKLRVLSRNQQliRLDFEEGFEGVDPEPLHErinqaLGNIGALVLSdyakgALASVQTMIQLARKAS 171
Cdd:cd01947 78 -KHTVAWRDKPTRKTLSFIDPNGE--RTITVPGERLEDDLKWPI-----LDEGDGVFIT-----AAAVDKEAIRKCRETK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190851 172 VPVLIDPKGTDFERY----RGATLLTPNLSEFEavagkcktEEELVERGMKIIADFelsaLLVTRSEQGMTLLqPGKAPL 247
Cdd:cd01947 145 LVILQVTPRVRVDELnqalIPLDILIGSRLDPG--------ELVVAEKIAGPFPRY----LIVTEGELGAILY-PGGRYN 211
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1513190851 248 HMPTQAQEVYDVTGAGDTVIGVLAATLAAGNSLEEACYFANAAAGVVVGKLG 299
Cdd:cd01947 212 HVPAKKAKVPDSTGAGDSFAAGFIYGLLKGWSIEEALELGAQCGAICVSHFG 263
|
|
| PRK00777 |
PRK00777 |
pantetheine-phosphate adenylyltransferase; |
343-397 |
9.82e-08 |
|
pantetheine-phosphate adenylyltransferase;
Pssm-ID: 234834 Cd Length: 153 Bit Score: 51.37 E-value: 9.82e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1513190851 343 VMTNGVFDILHAGHVSYLANARKLGDRLIVAVNSDASTKRLKgeTRPVNPLEQRM 397
Cdd:PRK00777 4 VAVGGTFDPLHDGHRALLRKAFELGKRVTIGLTSDEFAKSYK--KHKVRPYEVRL 56
|
|
| PRK11142 |
PRK11142 |
ribokinase; Provisional |
157-299 |
8.31e-07 |
|
ribokinase; Provisional
Pssm-ID: 236858 [Multi-domain] Cd Length: 306 Bit Score: 50.64 E-value: 8.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190851 157 LASVQTMIQLARKASVPVLIDP----KGTDfERYRGATLLTPNLSEFEAVAGKCKTEEELVERGMKIIADFELSALLVTR 232
Cdd:PRK11142 144 LETVLAAAKIAKQHGTKVILNPaparELPD-ELLALVDIITPNETEAEKLTGIRVEDDDDAAKAAQVLHQKGIETVLITL 222
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1513190851 233 SEQGMTLLQPGKAPLhMPTQAQEVYDVTGAGDTVIGVLAATLAAGNSLEEACYFANAAAGVVVGKLG 299
Cdd:PRK11142 223 GSRGVWLSENGEGQR-VPGFRVQAVDTIAAGDTFNGALVTALLEGKPLPEAIRFAHAAAAIAVTRKG 288
|
|
| MAK32 |
cd01943 |
MAK32 kinase. MAK32 is a protein found primarily in fungi that is necessary for the ... |
191-299 |
1.18e-06 |
|
MAK32 kinase. MAK32 is a protein found primarily in fungi that is necessary for the structural stability of L-A particles. The L-A virus particule is a specialized compartment for the transcription and replication of double-stranded RNA, known to infect yeast and other fungi. MAK32 is part of the host machinery used by the virus to multiply.
Pssm-ID: 238918 [Multi-domain] Cd Length: 328 Bit Score: 50.42 E-value: 1.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190851 191 LLTPNLSEFEAVAGkCKTEEELVERGmKIIADFELSALLVTRSEQGMTLLQPGK-----------APLHMP---TQAQEV 256
Cdd:cd01943 183 VFSPNLEEAARLLG-LPTSEPSSDEE-KEAVLQALLFSGILQDPGGGVVLRCGKlgcyvgsadsgPELWLPayhTKSTKV 260
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1513190851 257 YDVTGAGDTVIGVLAATLAAGNSLEEACYFANAAAGVVVGKLG 299
Cdd:cd01943 261 VDPTGGGNSFLGGFAAGLALTKSIDEACIYGSVAASFAIEQVG 303
|
|
| Phos_pyr_kin |
pfam08543 |
Phosphomethylpyrimidine kinase; This enzyme EC:2.7.4.7 is part of the Thiamine pyrophosphate ... |
151-287 |
1.29e-06 |
|
Phosphomethylpyrimidine kinase; This enzyme EC:2.7.4.7 is part of the Thiamine pyrophosphate (TPP) synthesis pathway, TPP is an essential cofactor for many enzymes.
Pssm-ID: 430062 [Multi-domain] Cd Length: 246 Bit Score: 49.40 E-value: 1.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190851 151 DYAK-GALASVQTMIQLA---RKASVPVLIDP----KGTD-------FERYRG-----ATLLTPNLSEFEAVAG-KCKTE 209
Cdd:pfam08543 62 DAVKtGMLGSAEIIEAVAeklDKYGVPVVLDPvmvaKSGDsllddeaIEALKEellplATLITPNLPEAEALTGrKIKTL 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190851 210 EELVERGmKIIADFELSALLVT------RSEQGMTLLQPGKAPLHMPTQAQEVYDVTGAGDTVIGVLAATLAAGNSLEEA 283
Cdd:pfam08543 142 EDMKEAA-KKLLALGAKAVLIKgghlegEEAVVTDVLYDGGGFYTLEAPRIPTKNTHGTGCTLSAAIAANLAKGLSLPEA 220
|
....
gi 1513190851 284 CYFA 287
Cdd:pfam08543 221 VREA 224
|
|
| Fructoselysine_kinase_like |
cd01940 |
Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a ... |
16-299 |
2.82e-06 |
|
Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a non-enzymatic reaction of glucose with a primary amine followed by an Amadori rearrangement, resulting in a protein that is modified at the amino terminus and at the lysine side chains. Fructoseamines are typically metabolized by fructoseamine-3-kinase, especially in higher eukaryotes. In E. coli, fructoselysine kinase has been shown in vitro to catalyze the phosphorylation of fructoselysine. It is proposed that fructoselysine is released from glycated proteins during human digestion and is partly metabolized by bacteria in the hind gut using a protein such as fructoselysine kinase. This family is found only in bacterial sequences, and its oligomeric state is currently unknown.
Pssm-ID: 238915 [Multi-domain] Cd Length: 264 Bit Score: 48.89 E-value: 2.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190851 16 VGDVMLDRYwygPTSRISpeapvpvvkvdtieeRPGG-AANVAMNIASLGAHSRLVGLTGIDDAARALSKSLADVNVKCD 94
Cdd:cd01940 5 IGDNVVDKY---LHLGKM---------------YPGGnALNVAVYAKRLGHESAYIGAVGNDDAGAHVRSTLKRLGVDIS 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190851 95 FVSVPTHPT-ITKLRVLSRNQQLIRLDFEEGFEGVDPEPLHERINQA-LGNIGALVLSDYAKGALASVQtmiqlarKASV 172
Cdd:cd01940 67 HCRVKEGENaVADVELVDGDRIFGLSNKGGVAREHPFEADLEYLSQFdLVHTGIYSHEGHLEKALQALV-------GAGA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190851 173 PVLID--PKGTDFEryrgATLLTPNLsefEAVAGKCKTE-EELVERGMKIIADFELSALLVTRSEQGMTLLQpGKAPLHM 249
Cdd:cd01940 140 LISFDfsDRWDDDY----LQLVCPYV---DFAFFSASDLsDEEVKAKLKEAVSRGAKLVIVTRGEDGAIAYD-GAVFYSV 211
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1513190851 250 PTQAQEVYDVTGAGDTVI-GVLAATLAAGNSLEEACYFANAAAGVVVGKLG 299
Cdd:cd01940 212 APRPVEVVDTLGAGDSFIaGFLLSLLAGGTAIAEAMRQGAQFAAKTCGHEG 262
|
|
| ribokinase_group_D |
cd01937 |
Ribokinase-like subgroup D. Found in bacteria and archaea, this subgroup is part of the ... |
40-295 |
2.89e-06 |
|
Ribokinase-like subgroup D. Found in bacteria and archaea, this subgroup is part of the ribokinase/pfkB superfamily. Its oligomerization state is unknown at this time.
Pssm-ID: 238912 [Multi-domain] Cd Length: 254 Bit Score: 48.55 E-value: 2.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190851 40 VVKVDTIEERPGGAANVAMNIAS-LGAHSRLVGLTGIDDAARalsKSLADVNVKcDFVSVPTHPTIT-KLRVLSRNQQLI 117
Cdd:cd01937 13 IVTNGSGVVKPGGPATYASLTLSrLGLTVKLVTKVGRDYPDK---WSDLFDNGI-EVISLLSTETTTfELNYTNEGRTRT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190851 118 RLdfeegfegVDPEPLHERINQALGNIGALVLsdyakgaLASV-QTMIQLARKASVPVLIDPKG-----TDFERYRGATL 191
Cdd:cd01937 89 LL--------AKCAAIPDTESPLSTITAEIVI-------LGPVpEEISPSLFRKFAFISLDAQGflrraNQEKLIKCVIL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190851 192 LTP---NLSEFEAVagKCKTEEELVergmKIIADFELSALLVTRSEQGMTLLQpGKAPLHMPTQAQEVYDVTGAGDTVIG 268
Cdd:cd01937 154 KLHdvlKLSRVEAE--VISTPTELA----RLIKETGVKEIIVTDGEEGGYIFD-GNGKYTIPASKKDVVDPTGAGDVFLA 226
|
250 260
....*....|....*....|....*..
gi 1513190851 269 VLAATLAAGNSLEEACYFANAAAGVVV 295
Cdd:cd01937 227 AFLYSRLSGKDIKEAAEFAAAAAAKFI 253
|
|
| PRK09850 |
PRK09850 |
pseudouridine kinase; Provisional |
46-287 |
5.59e-05 |
|
pseudouridine kinase; Provisional
Pssm-ID: 182111 [Multi-domain] Cd Length: 313 Bit Score: 44.98 E-value: 5.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190851 46 IEERPGGAA-NVAMNIASLGAHSRLVGLTGIDDAARAL--SKSLADVNV-KCdfVSVPTHPTITKLRVLSRN-QQLIRLD 120
Cdd:PRK09850 35 IKFTPGGVGrNIAQNLALLGNKAWLLSAVGSDFYGQSLltQTNQSGVYVdKC--LIVPGENTSSYLSLLDNTgEMLVAIN 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190851 121 FEEGFEGVDPEPLHERINQALGNIGALVLSDYAKGALASVqtmiqLARKASVPVLIDPK-----GTDFERYRGATLLTPN 195
Cdd:PRK09850 113 DMNISNAITAEYLAQHREFIQRAKVIVADCNISEEALAWI-----LDNAANVPVFVDPVsawkcVKVRDRLNQIHTLKPN 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190851 196 LSEFEAVAGKCKTEEELVERGMKIIADFELSALLVTRSEQGMTLLQ-PGKAPLHMPTQAQeVYDVTGAGDTVIGVLAATL 274
Cdd:PRK09850 188 RLEAETLSGIALSGREDVAKVAAWFHQHGLNRLVLSMGGDGVYYSDiSGESGWSAPIKTN-VINVTGAGDAMMAGLASCW 266
|
250
....*....|...
gi 1513190851 275 AAGNSLEEACYFA 287
Cdd:PRK09850 267 VDGMPFAESVRFA 279
|
|
| Ketohexokinase |
cd01939 |
Ketohexokinase (fructokinase, KHK) catalyzes the phosphorylation of fructose to ... |
226-300 |
9.93e-05 |
|
Ketohexokinase (fructokinase, KHK) catalyzes the phosphorylation of fructose to fructose-1-phosphate (F1P), the first step in the metabolism of dietary fructose. KHK can also phosphorylate several other furanose sugars. It is found in higher eukaryotes where it is believed to function as a dimer and requires K(+) and ATP to be active. In humans, hepatic KHK deficiency causes fructosuria, a benign inborn error of metabolism.
Pssm-ID: 238914 [Multi-domain] Cd Length: 290 Bit Score: 44.32 E-value: 9.93e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1513190851 226 SALLVTRSEQGMTLLQPGKAPLHMPTQAQE-VYDVTGAGDT-VIGVLAATLAAGNSLEEACYFANAAAGVVVGKLGT 300
Cdd:cd01939 213 ALLVCTWGDQGAGALGPDGEYVHSPAHKPIrVVDTLGAGDTfNAAVIYALNKGPDDLSEALDFGNRVASQKCTGVGF 289
|
|
| PanC |
COG0414 |
Panthothenate synthetase [Coenzyme transport and metabolism]; Panthothenate synthetase is part ... |
326-372 |
2.71e-03 |
|
Panthothenate synthetase [Coenzyme transport and metabolism]; Panthothenate synthetase is part of the Pathway/BioSystem: Pantothenate/CoA biosynthesis
Pssm-ID: 440183 [Multi-domain] Cd Length: 280 Bit Score: 39.63 E-value: 2.71e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1513190851 326 DELKVAVAAARKRGEKV--VMTNGVfdiLHAGHVSYLANARKLGDRLIV 372
Cdd:COG0414 8 AELRAALAAWRAAGKRIglVPTMGA---LHEGHLSLVRRARAEADVVVV 53
|
|
| PRK06427 |
PRK06427 |
bifunctional hydroxy-methylpyrimidine kinase/ hydroxy-phosphomethylpyrimidine kinase; Reviewed |
189-287 |
2.88e-03 |
|
bifunctional hydroxy-methylpyrimidine kinase/ hydroxy-phosphomethylpyrimidine kinase; Reviewed
Pssm-ID: 180561 [Multi-domain] Cd Length: 266 Bit Score: 39.34 E-value: 2.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190851 189 ATLLTPNLSEFEAVAG-KCKTEEELVERGMKIIADFELSALLVTrseqGMTLLQPGKAP--LHMPTQAQEV-------YD 258
Cdd:PRK06427 134 ATLITPNLPEAEALTGlPIADTEDEMKAAARALHALGCKAVLIK----GGHLLDGEESVdwLFDGEGEERFsapriptKN 209
|
90 100
....*....|....*....|....*....
gi 1513190851 259 VTGAGDTVIGVLAATLAAGNSLEEACYFA 287
Cdd:PRK06427 210 THGTGCTLSAAIAAELAKGASLLDAVQTA 238
|
|
| Pantoate_ligase |
pfam02569 |
Pantoate-beta-alanine ligase; Pantoate-beta-alanine ligase, also know as pantothenate synthase, ... |
326-375 |
4.70e-03 |
|
Pantoate-beta-alanine ligase; Pantoate-beta-alanine ligase, also know as pantothenate synthase, (EC:6.3.2.1) catalyzes the formation of pantothenate from pantoate and alanine.
Pssm-ID: 460595 [Multi-domain] Cd Length: 277 Bit Score: 38.94 E-value: 4.70e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1513190851 326 DELKVAVAAARKRGEKV--VMTNGVfdiLHAGHVSYLANARKLGDRLIVA--VN 375
Cdd:pfam02569 7 AELRAWLRAWRRAGKTIglVPTMGA---LHEGHLSLVRRARAENDVVVVSifVN 57
|
|
| pyridoxal_pyridoxamine_kinase |
cd01173 |
Pyridoxal kinase plays a key role in the synthesis of the active coenzyme pyridoxal-5 ... |
139-284 |
5.72e-03 |
|
Pyridoxal kinase plays a key role in the synthesis of the active coenzyme pyridoxal-5'-phosphate (PLP), by catalyzing the phosphorylation of the precursor vitamin B6 in the presence of Zn2+ and ATP. Mammals are unable to synthesize PLP de novo and require its precursors in the form of vitamin B6 (pyridoxal, pyridoxine, and pyridoxamine) from their diet. Pyridoxal kinase encoding genes are also found in many other species including yeast and bacteria.
Pssm-ID: 238578 [Multi-domain] Cd Length: 254 Bit Score: 38.33 E-value: 5.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190851 139 QALGNIGAL-----VLSDYAKGA--LASVQTMIQLARKAS--VPVLIDP------KGTDF-----ERYR-----GATLLT 193
Cdd:cd01173 62 EGLEALGLLleydaVLTGYLGSAeqVEAVAEIVKRLKEKNpnLLYVCDPvmgdngKLYVVaeeivPVYRdllvpLADIIT 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190851 194 PNLSEFEAVAG-KCKTEEELVE-------RGMKII--------ADFELSALLVTRSEQGMtllqpgkapLHMPTQAQEVY 257
Cdd:cd01173 142 PNQFELELLTGkKINDLEDAKAaaralhaKGPKTVvvtsvelaDDDRIEMLGSTATEAWL---------VQRPKIPFPAY 212
|
170 180
....*....|....*....|....*..
gi 1513190851 258 dVTGAGDTVIGVLAATLAAGNSLEEAC 284
Cdd:cd01173 213 -FNGTGDLFAALLLARLLKGKSLAEAL 238
|
|
| YXKO-related |
cd01171 |
B.subtilis YXKO protein of unknown function and related proteins. Based on the conservation of ... |
155-292 |
6.96e-03 |
|
B.subtilis YXKO protein of unknown function and related proteins. Based on the conservation of the ATP binding site, the substrate binding site and the Mg2+binding site and structural homology this group is a member of the ribokinase-like superfamily.
Pssm-ID: 238576 Cd Length: 254 Bit Score: 38.36 E-value: 6.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190851 155 GALASVQTMIQLARKASVPVLID-------PKGTDFERYRGATLLTPNLSEFEAVAGkCKTEEELVERgmkIIADFELSA 227
Cdd:cd01171 88 GRDEEAAEILEKALAKDKPLVLDadalnllADEPSLIKRYGPVVLTPHPGEFARLLG-ALVEEIQADR---LAAAREAAA 163
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1513190851 228 LL-----------VTRSEQGMTLLQPGKAPLhmptQAqevydVTGAGDTVIGVLAATLAAGNSLEEACY---FANAAAG 292
Cdd:cd01171 164 KLgatvvlkgavtVIADPDGRVYVNPTGNPG----LA-----TGGSGDVLAGIIAALLAQGLSPLEAAAlavYLHGLAG 233
|
|
| |
